The GTPase activity of murine guanylate-binding protein 2 (mGBP2) controls the intracellular localization and recruitment to the parasitophorous vacuole of Toxoplasma gondii.

@article{Kravets2012TheGA,
  title={The GTPase activity of murine guanylate-binding protein 2 (mGBP2) controls the intracellular localization and recruitment to the parasitophorous vacuole of Toxoplasma gondii.},
  author={Elisabeth Kravets and Daniel Degrandi and Stefanie Weidtkamp-Peters and Britta Ries and Carolin Konermann and Suren Felekyan and Julia M Dargazanli and Gerrit J. K. Praefcke and Claus A M Seidel and Lutz Schmitt and Sander H. J. Smits and Klaus Pfeffer},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 33},
  pages={27452-66}
}
One of the most abundantly IFN-γ-induced protein families in different cell types is the 65-kDa guanylate-binding protein family that is recruited to the parasitophorous vacuole of the intracellular parasite Toxoplasma gondii. Here, we elucidate the relationship between biochemistry and cellular host defense functions of mGBP2 in response to Toxoplasma gondii. The wild type protein exhibits low affinities to guanine nucleotides, self-assembles upon GTP binding, forming tetramers in the… CONTINUE READING
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